ID A0A1B9IK01_9TREE Unreviewed; 904 AA.
AC A0A1B9IK01;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Elongation factor 1 alpha-like protein {ECO:0000313|EMBL:OCF55872.1};
GN ORFNames=L486_06628 {ECO:0000313|EMBL:OCF55872.1};
OS Kwoniella mangroviensis CBS 10435.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1331196 {ECO:0000313|EMBL:OCF55872.1, ECO:0000313|Proteomes:UP000092583};
RN [1] {ECO:0000313|EMBL:OCF55872.1, ECO:0000313|Proteomes:UP000092583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10435 {ECO:0000313|EMBL:OCF55872.1,
RC ECO:0000313|Proteomes:UP000092583};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Kwoniella mangroviensis CBS10435.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10435 {ECO:0000313|Proteomes:UP000092583};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KI669465; OCF55872.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B9IK01; -.
DR STRING; 1331196.A0A1B9IK01; -.
DR Proteomes; UP000092583; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01883; EF1_alpha; 1.
DR CDD; cd16267; HBS1-like_II; 1.
DR CDD; cd04093; HBS1_C_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR015033; HBS1-like_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR PANTHER; PTHR23115:SF188; HBS1-LIKE PROTEIN; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR Pfam; PF08938; HBS1_N; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:OCF55872.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:OCF55872.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092583};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT DOMAIN 472..697
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 97559 MW; 35BD713A12EF29D3 CRC64;
MSRHRFVRNM DLDDEMNEEE EEGYSQEEQA QMASAMPVAR NALKDIKPPI SDDAIADSLW
HYWFDVEKAV HWLRQDHEKK GEAPHPSLRP TPKEQPRRRP KNLFSSKPSS SSSSDSPQPP
LTALQRLSLS RKQATSSSPS SSPAPTATAV SSNENGAKPM SKLALLAQKR KEAAAAAAGQ
SAENPLRTPT KSPSSSTPAS GTQSPNSDTA SKPSSKLAQK MAAARAAREE SAAKAAPTPL
SEDTMAIDEP NSTSTVQDDL DIFSAFTVPQ THKSHSSSSS PSTFFSILTS TSSADQSKTD
MEITNLHVPL ATDISALTKR FEEAFAESPD EVVLRKRQGR AVMVKCRIER YTFGLRSAKA
ASVSQKSASL PGKPRTQTGT TPKSKLQPKT QPNSPVNSTS KAGSSGTSTP TNKGSGSKSP
LTVAQQDLAG LHLDQEVDLE VEKEKYKESA ALSMKTEELI AKVRKEEEES GKKNISMIVV
GHVDAGKSTL MGRLLYDIGE LSEKEKTANE RGSKKIGKGS FAFAWGLDAL GDERDRGVTI
DIATTHFTTP HRNYTLLDAP GHRDFIPAMI SGAAQADVAL MVVDGSPGEF EAGFERGGQT
REHAWLVRSL GVKEIIVGIN KMDLVSWSQD RYEEIVEALK PFLLSAGFAS AKTTFMPLAA
MEGINILEND VEELKEWYDG PTLINALDKV EVPSRPYESP LRIPVSNVFK GQTAVASGVA
VSGRLCSGVV QVGDRLRAIP GDEVATVRTI EVDEDSAPYA VSGQNVTLYL SGIDSINLSI
GTILCPTSLP VPLVSKFTTQ ILVFDLQSPI IIGTSVELFH HSVNLPATIS RLINVLEKGQ
VTKKNPRVLQ KGMTATIEIT LRSTSNNNAR IPIETSQQNK EMGRVLIRRN GETIAAGVVT
ELLG
//
